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Area of Science:

  • Proteomics
  • Molecular Biology
  • Biochemistry

Background:

  • Alternative translation initiation and splicing create N-terminal proteoforms.
  • These proteoforms can exhibit different localizations, stabilities, and functions compared to canonical proteins.
  • The engagement of N-terminal proteoforms in distinct protein complexes was previously understudied.

Purpose of the Study:

  • To investigate the extent to which N-terminal proteoforms engage in different protein complexes compared to their canonical counterparts.
  • To map the interactomes of selected N-terminal proteoform pairs and their canonical forms.
  • To assess the biological relevance of N-terminal proteoforms through tissue expression analysis.

Main Methods:

  • Generation of a comprehensive catalog of N-terminal proteoforms in HEK293T cellular cytosol.
  • Selection of 22 N-terminal proteoform pairs for interactome profiling.
  • Protein-protein interaction profiling and analysis of interactome overlap and differences.

Main Results:

  • High overlap in interactomes between N-terminal proteoforms and their canonical counterparts was observed, indicating functional relationships.
  • N-terminal proteoforms demonstrated the ability to form new interactions and lose existing ones compared to canonical forms.
  • Evidence for the expression of N-terminal proteoforms across various human tissues, including tissue-specific patterns, was provided.

Conclusions:

  • N-terminal proteoforms contribute to proteome functional diversity through altered protein-protein interactions.
  • The study highlights the biological relevance of N-terminal proteoforms, supported by their presence in different human tissues.
  • Understanding N-terminal proteoform interactomes is crucial for comprehending the full functional capacity of proteomes.